Answer:
Explanation:
1. charge in trypsin
: two other molecules in elastase
2. Chymotrypsin cleaves peptide bonds after bulky or aromatic side chains, such as those of the amino acids phenylalanine or tyrosine. The specificity pocket, or substrate-binding site, is deep and has hydrophobic side chains.
Trypsin cleaves peptide bonds following basic amino acid side chains. Lysine and arginine both have basic amino acid side chains that are positively charged at pH 7. Trypsin's substrate-binding site contains a negatively charged amino acid residue.
Elastase cleaves peptide bonds after amino acids with small side chains, such as glycine, alanine, or valine. The specificity pocket for elastase has bulky side chains that block larger amino acid side chains, but can accomodate smaller side chains, such as the -H, -CH3, and -CH(CH3)2 side chains of glycine, alanine, and valine, respectively.
3. Their binding pockets
- trypsin = long & (-) D on bottom
- chymotrypsin = deep & wide
- elastase = aliphatic a.a. = shallow
Answer:
Between mars and Jupiter
Explanation:
between mars and jupiter is where the astriod belt is located. (between the rock and gas planets)
What causes people to be color-blind
can be tested scientifically
<span>Estoy 50% seguro de que la respuesta es profase</span>
here are the structures i hope it helps
Answer:
primary, secondary, tertiary, and quaternary.
